ID   W0U5W9_9FIRM            Unreviewed;       278 AA.
AC   W0U5W9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:CCO05155.1};
DE            EC=1.3.1.12 {ECO:0000313|EMBL:CCO05155.1};
GN   Name=tyrA {ECO:0000313|EMBL:CCO05155.1};
GN   ORFNames=RBI_I01452 {ECO:0000313|EMBL:CCO05155.1};
OS   Ruminococcus bicirculans (ex Wegman et al. 2014).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1160721 {ECO:0000313|EMBL:CCO05155.1, ECO:0000313|Proteomes:UP000027600};
RN   [1] {ECO:0000313|EMBL:CCO05155.1, ECO:0000313|Proteomes:UP000027600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=80/3 {ECO:0000313|EMBL:CCO05155.1};
RX   PubMed=23919528; DOI=10.1111/1462-2920.12217;
RA   Wegmann U., Louis P., Goesmann A., Henrissat B., Duncan S.H., Flint H.J.;
RT   "Complete genome of a new Firmicutes species belonging to the dominant
RT   human colonic microbiota ('Ruminococcus bicirculans') reveals two
RT   chromosomes and a selective capacity to utilize plant glucans.";
RL   Environ. Microbiol. 16:2879-2890(2014).
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR   EMBL; HF545616; CCO05155.1; -; Genomic_DNA.
DR   RefSeq; WP_038672055.1; NZ_HF545616.1.
DR   AlphaFoldDB; W0U5W9; -.
DR   STRING; 1160721.RBI_I01452; -.
DR   GeneID; 41519494; -.
DR   KEGG; rus:RBI_I01452; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_2_0_9; -.
DR   OrthoDB; 9802008at2; -.
DR   Proteomes; UP000027600; Chromosome I.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046825; PDH_C.
DR   InterPro; IPR046826; PDH_N.
DR   InterPro; IPR003099; Prephen_DH.
DR   PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF20463; PDH_C; 1.
DR   Pfam; PF02153; PDH_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CCO05155.1}.
FT   DOMAIN          1..278
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   278 AA;  30178 MW;  5BAD11E73A7D9277 CRC64;
     MKICIVGLGL IGGSLAKAIK KNTHESCFGI DIDRGTIAGA LAQEAIDGEM TIDDLAGCDV
     VIVGLHPEAT IKFITENAGK FKKGGIVLDT CGVKGEIVRA VEGVCIENGV NFLGCHPMAG
     REFSGFAYSV DNLFEKASFI MTPTDRTPMR VVQDISRLAY NIGFAKVVVS NVKEHDSVIA
     FTSQLAHVVS SSYVKSPSLL KQAGFSAGSF KDLTRVAKLN EDMWTELFLM NRGPLVDEIE
     HIIARLTEYR DAIANNDAQR LHDLLKEGRE LKELSNNS
//